Results 181 to 190 of about 41,395 (219)

Immune response with long-term memory triggered by amorphous aggregates of misfolded anti-EGFR VHH-7D12 is directed against the native VHH-7D12 as well as the framework of the analogous VHH-9G8

European Journal of Pharmaceutics and Biopharmaceutics, 2021
We previously demonstrated that amorphous aggregates of misfolded VHH-7D12 antibodies (VHH-Mis), a potential anti-EGFR drug, can generate a robust serum IgG response. Here we investigate the immunogenic nature, especially the specificity of the immune response induced by VHH-Mis. To this end, we used two natively folded and 77% identical anti-EGFR VHHs
Md, Golam Kibria, Yoko, Akazawa-Ogawa, Yoshihisa, Hagihara, Yutaka, Kuroda   +3 more
openaire   +2 more sources

Quality assessment of VHH models

Journal of Biomolecular Structure and Dynamics, 2023
Heavy Chain Only Antibodies are specific to Camelid species. Despite the lack of the light chain variable domain, their heavy chain variable domain (VH) domain, named VHH or nanobody, has promising potential applications in research and therapeutic ...
A. Nadaradjane, J. Diharce, Joseph Rebehmed, F. Cadet, F. Gardebien, Jean-Christophe Gelly, C. Etchebest, A. D. de Brevern   +7 more
semanticscholar   +1 more source

Expression of VHHs in Saccharomyces cerevisiae

2012
The production of VHHs in microorganisms is relatively straightforward, however the amount of VHH produced per volume unit can vary substantially from hardly detectable to hundreds of milligrams per liter. Expression in Escherichia coli is more commonly used at initial research phase, since production of VHHs for large-scale application in E.
Andrea, Gorlani, Hans, de Haard, Theo, Verrips   +2 more
openaire   +2 more sources

A disposable VHH-based SPR fiber probe for sensitive and specific detection of MMP-9 in cancer and inflammatory disease.

Biosensors & bioelectronics
A novel one-step label-free immunoassay platform was developed through the integration of nanobody (VHH) technology with a disposable surface plasmon resonance (SPR) fiber probe for rapid, precise biomarker detection.
Dandan Wu, Jian Yang, Junxiao Cong, Jian Zhou, Youbin Li, Feng Yan, Xuejin Li, Yuzhi Chen, Liang Ye   +8 more
semanticscholar   +1 more source

Developing drug-like single-domain antibodies (VHH) from in vitro libraries

mAbs
Here, we describe a new VHH library for therapeutic discovery which optimizes humanness, stability, affinity, diversity, developability, and facile purification using protein A in the absence of an Fc domain.
M. Erasmus, Andre A R Teixeira, Esteban Molina, Luis Antonio Rodriguez Carnero, Jianquan Li, David Knight, R. Di Niro, Camila Leal-Lopes, A. Fanni, Hallie Troell, Ashley DeAguero, Laura Spector, S. D’Angelo, F. Ferrara, A. R. Bradbury   +14 more
semanticscholar   +1 more source

Affinity‐stability trade‐off mechanism of residue 35 in framework region 2 of VHH antibodies with β‐hairpin CDR3

Protein Science
Single‐domain VHH antibodies are promising therapeutic and diagnostic tools. The third complementarity‐determining region (CDR3) is usually the most critical region for antigen recognition by VHH antibodies.
Koichi Yamamoto, S. Nagatoishi, Ryo Matsunaga, Makoto Nakakido, Daisuke Kuroda, Kouhei Tsumoto   +5 more
semanticscholar   +1 more source

Selection of VHHs Under Application Conditions

2012
The successful application of antibody fragments such as VHHs in diagnostic assays, affinity purification, imaging, or therapy is not determined by the specificity and affinity of the antibody fragment alone. The ability to bind the target protein in the environment in which the antibody fragment is intended to functionally perform determines to a ...
Dolk, E., Verrips, C.T., de Haard, J.J.W.   +2 more
openaire   +3 more sources

Development of a novel anti-CEACAM5 VHH for SPECT imaging and potential cancer therapy applications

European Journal of Nuclear Medicine and Molecular Imaging
In this study, we investigated the utility of a novel developed anti-CEACAM5 VHH for cancer diagnosis and its potential of being a targeting-moiety of VHH-drug conjugates for cancer therapy.
Ying Cong, R. Biemans, N. Lieuwes, Dennis Suijlen, P. Lambin, Ingrid Dijkgraaf, Matthias Bauwens, A. Yaromina, L. J. Dubois   +8 more
semanticscholar   +1 more source

Evaluation of an anti-CD3 VHH and construction of an anti-CD3/anti-EGFR bispecific tandem VHH as a cancer cell targeting drug construct

Biochemistry and Biophysics Reports
Recently, the development of T-cell engager cancer therapeutics, consisting of anticancer and anti-T-cell antibody parts to engage the T-cell to the cancer site, has gained interest.
Takuya Asanuma, Peiwei Ding, Yuki Kato, Takeshi Nakanishi, R. Asano, Koki Makabe   +5 more
semanticscholar   +1 more source

Lateral recognition of a dye hapten by a llama VHH domain

Journal of Molecular Biology, 2001
Camelids, camels and llamas, have a unique immune system able to produce heavy-chain only antibodies. Their VH domains (VHHs) are the smallest binding units produced by immune systems, and therefore suitable for biotechnological applications through heterologous expression.
Silvia Spinelli, Mariella Tegoni, Leon Frenken   +2 more
exaly   +3 more sources